Studying the Folding Behavior of a 3D Lattice Protein under Oscillatory Conditions

By spontaneously and reliably folding from a primary amino acid sequence into a highly specific native geometry with bioactive functionalities, the natively-folded protein plays a significant role in fundamental biological processes. Protein folding is governed by the interactions between residues and between residues and the environment. The structural stability and bio-functionality of proteins depend on physiological environmental factors, such as temperature, acidity, crowding, and ionic strength. In addition, the local cellular environment is highly dynamic -- both spatially and temporally heterogeneous. In this work, we employed a 3D lattice protein model to investigate the changes to the equilibrium folded state properties and to the kinetics of folding pathways for small proteins that fold amidst ongoing temperature oscillations